Study on interactions of cationic gemini surfactants with folded and unfolded bovine serum albumin: Effect of spacer group of surfactants

SONU, .; Halder, Sayantan; Kumari, Suman; Aggrawal, Rishika; Aswal, Vinod K.; Saha, Sarani

doi:10.1016/j.molliq.2017.07.122

Cited by 24 publications

(15 citation statements)

References 58 publications

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“…However, we did not notice any significant change for 12-8-12, which could be because a surfactant with a long spacer chain interacts less effectively at a low concentration range with the protein. 38 Therefore, the effect on fluorescence intensity because of a slightly higher hydrophobicity imparted to the native BSA as a result of binding of a few surfactant molecules cannot be ruled out. On further increase in the concentration of surfactant, the protein molecules get unfolded.…”

Section: Results and Discussionmentioning

confidence: 99%

“…When doing this study with a high concentration of BSA, we found some differences as compared to our previous study with a low concentration of BSA. 38 With a high concentration of BSA, we have found the expulsion of some percentage of DMASBT molecules from beads, that is, micelles with the addition of a high concentration of gemini surfactants.…”

Section: Introductionmentioning

confidence: 89%

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Fluorescence Resonance Energy Transfer, Small-Angle Neutron Scattering, and Dynamic Light Scattering Study on Interactions of Gemini Surfactants Having Different Spacer Groups with Protein at Various Regions of Binding Isotherms

et al. 2018

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The binding interactions of three gemini surfactants having different spacer groups (12-4-12, 12-8-12, and 12-4(OH)-12) with a high concentration (150 μM) of bovine serum albumin (BSA) at various regions of binding isotherms have been studied by means of steady-state fluorescence and fluorescence anisotropy, time-correlated single-photon counting fluorescence of trans -2-[4-(dimethylamino)styryl]benzothiazole, small-angle neutron scattering (SANS), and dynamic light scattering (DLS) measurements. The fluorescence resonance energy transfer phenomenon between the twisted intramolecular charge transfer fluorescent molecule, trans -2-[4-(dimethylamino)styryl]benzothiazole as an acceptor, and tryptophan 213 (Trp-213) of BSA as a donor has been successfully used to probe the binding interactions of gemini surfactants with protein at all regions of binding isotherms. The increasing order of energy transfer efficiency at a higher concentration range of surfactants is 12-8-12 > 12-4-12 > 12-4(OH)-12. Stronger binding of micelles of gemini surfactant molecules having a comparatively more hydrophobic spacer group with the hydrophobic segments of the protein results in closer approach of trans -2-[4-(dimethylamino)styryl]benzothiazole molecules solubilized in micelles to Trp-213. The average excited-state lifetimes become shorter with a trend of increase in contribution from the fast component and decrease in contribution from the slow component to the decay with increasing concentration of a surfactant. The nonradiative rate constant of trans -2-[4-(dimethylamino)styryl]benzothiazole increases with increasing concentration of a surfactant because the average microenvironment around it in protein–surfactant aggregates is more polar as compared to that in native protein. SANS and DLS measurements were carried out for the study of the structural deformations in the protein, on enhancement of the concentration of the gemini surfactants. The necklace and bead model has been used for the analysis of SANS data for the protein–surfactant complexes. At a higher concentration range, 12-8-12 and 12-4-12 have a slightly smaller fractal dimension and a larger correlation length as compared to 12-4(OH)-12. DLS data show that the increasing order of hydrodynamic diameter for the complexes of protein with three gemini surfactants in their high concentration range is 12-4(OH)-12 < 12-4-12 < 12-8-12.

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Section: Results and Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 89%

Fluorescence Resonance Energy Transfer, Small-Angle Neutron Scattering, and Dynamic Light Scattering Study on Interactions of Gemini Surfactants Having Different Spacer Groups with Protein at Various Regions of Binding Isotherms

et al. 2018

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“…Despite their importance in several industrial fields, studies of Protein-Gemini surfactants interactions are limited, compared with those conducted with single chain surfactants (Sinha et al 2016 ; Parray et al 2018 ; Akram et al 2019 ). Several studies have revealed that some interaction mechanisms of these new generation of surfactants with proteins are shared with their corresponding monomers differing in the effects that they induce in the biomolecule, ranging from having stronger molecular interactions than their monomeric counterpart to changes or stabilization in the secondary and tertiary structures of proteins (Sinha et al 2016 ; Sonu et al 2017 ; Akram et al 2019 ). Comparative studies of the interaction of BSA with the cationic surfactant Dodecyl Trimethyl Ammonium Bromide (DTAB) and with three Gemini-surfactants of the bis(dimethyldodecylammonium bromide) family; butanediyl-1,4-bis(dimethyldodecylammonium bromide (12–4-12,2Br −), 2-butanol-1,4-bis(dimethyldodecylammonium bromide) (12–4(OH)-12,2Br −), 2,4-dibutanol-1,4-bis(dimethyldodecylammonium bromide) (12-4(OH)2-12,2Br −), showed that at lower concentrations of the surfactant the interaction in the surfactant–protein complex is managed by electrostatic forces and while the concentration of the surfactant increases.…”

Section: Surfactant–protein Interactionsmentioning

confidence: 99%

“…The union of the protein with the surfactant is hydrophobic in nature, which is stronger with the Gemini-surfactant, causing greater denaturation of BSA compared to DTAB, which suggests that the spacer between the two monomers plays an important role (Sinha et al 2016 ). Sonu et al ( 2017 ) conducted a study on the effect of surfactant spacers [12-8-12, 2Br-], [12-4-12, 2Br-] and [12-4 (OH) -12, 2Br-] on the interaction with BSA and reported that the more hydrophobic the spacer is, the lower is the reduction in the number of α-helices and denaturing effects. Akram et al ( 2019 ) on the other hand, analysed the interaction of the BSA model protein with three members of a family of Gemini Cm-E20-Cm surfactants and demonstrated that the binding of these dimeric surfactants with the protein is considerably strong, without causing a significant loss of α-helix (3–4%), keeping the secondary and tertiary structure of the BSA virtually intact.…”

Section: Surfactant–protein Interactionsmentioning

confidence: 99%

Surfactants: physicochemical interactions with biological macromolecules

et al. 2021

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Macromolecules are essential cellular components in biological systems responsible for performing a large number of functions that are necessary for growth and perseverance of living organisms. Proteins, lipids and carbohydrates are three major classes of biological macromolecules. To predict the structure, function, and behaviour of any cluster of macromolecules, it is necessary to understand the interaction between them and other components through basic principles of chemistry and physics. An important number of macromolecules are present in mixtures with surfactants, where a combination of hydrophobic and electrostatic interactions is responsible for the specific properties of any solution. It has been demonstrated that surfactants can help the formation of helices in some proteins thereby promoting protein structure formation. On the other hand, there is extensive research towards the use of surfactants to solubilize drugs and pharmaceuticals; therefore, it is evident that the interaction between surfactants with macromolecules is important for many applications which includes environmental processes and the pharmaceutical industry. In this review, we describe the properties of different types of surfactants that are relevant for their physicochemical interactions with biological macromolecules, from macromolecules–surfactant complexes to hydrophobic and electrostatic interactions.

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“…Two peaks are observed in the spectra, one in the far UV, at 210 nm, and another in the near UV, at 280 nm. The first one is associated to transitions in the polypeptide's backbone structure, and it is characteristic of the specific protein; the second one comes from the transition in the amino acids, and it is typically used to determine the protein concentration [14]. In the studied concentration range, the intensities of this second peak follow the Beer-Lambert law (Figure 2c inset), which we thus use to determine the concentration of the filtered protein suspensions.…”

Section: Dynamic Light Scattering Of Gold Nanoparticles and Proteinsmentioning

confidence: 99%

Towards Standards for Light Scattering Studies of Proteins Stability and Nanoparticle-Protein Interactions

Frau

Schintke

2020

2020 22nd International Conference on Transparent Optical Networks (ICTON)

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Protein-nanoparticle suspensions are nowadays widely studied for the development of medical and environmental biosensors. The complexity of interactions between nanoparticles and biological fluids, together with the increasing use of dynamic light scattering (DLS) for their characterization, support the need to develop common standards for DLS measurements and analysis, in order to enable a reliable comparison of measurement results. In this study, we use 3D cross-correlation Dynamic Light Scattering (3Dcc-DLS) for the characterization of gold nanoparticles (Au NP), with spherical and rod shape, stabilized with sodium citrate, and their interaction with bovine serum albumin (BSA). We show that for Au nanorods it is possible to distinguish the rotational and translational motion. Moreover, we monitor the interaction of Au NPs and BSA over time, in order to analyse the first step of protein corona formation. Our results show that Au nanorods interact more than Au nanospheres with BSA. From the evolution of the rotational and translational peaks we conclude that the proteins tend to bind on the long cylindrical side of the nanorods.

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Study on interactions of cationic gemini surfactants with folded and unfolded bovine serum albumin: Effect of spacer group of surfactants

Cited by 24 publications

References 58 publications

Fluorescence Resonance Energy Transfer, Small-Angle Neutron Scattering, and Dynamic Light Scattering Study on Interactions of Gemini Surfactants Having Different Spacer Groups with Protein at Various Regions of Binding Isotherms

Fluorescence Resonance Energy Transfer, Small-Angle Neutron Scattering, and Dynamic Light Scattering Study on Interactions of Gemini Surfactants Having Different Spacer Groups with Protein at Various Regions of Binding Isotherms

Surfactants: physicochemical interactions with biological macromolecules

Towards Standards for Light Scattering Studies of Proteins Stability and Nanoparticle-Protein Interactions

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